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3WUI

Dimeric horse cytochrome c formed by refolding from molten globule state

Summary for 3WUI
Entry DOI10.2210/pdb3wui/pdb
Related3WC8
DescriptorCytochrome c, HEME C, TETRAETHYLENE GLYCOL, ... (6 entities in total)
Functional Keywordselectron transport
Biological sourceEquus caballus (horse)
Total number of polymer chains1
Total formula weight12845.54
Authors
Deshpande, M.S.,Parui, P.P.,Kamikubo, H.,Yamanaka, M.,Nagao, S.,Komori, H.,Kataoka, M.,Higuchi, Y.,Hirota, S. (deposition date: 2014-04-25, release date: 2014-07-16, Last modification date: 2024-11-20)
Primary citationDeshpande, M.S.,Parui, P.P.,Kamikubo, H.,Yamanaka, M.,Nagao, S.,Komori, H.,Kataoka, M.,Higuchi, Y.,Hirota, S.
Formation of domain-swapped oligomer of cytochrome C from its molten globule state oligomer.
Biochemistry, 53:4696-4703, 2014
Cited by
PubMed Abstract: Many proteins, including cytochrome c (cyt c), have been shown to form domain-swapped oligomers, but the factors governing the oligomerization process remain unrevealed. We obtained oligomers of cyt c by refolding cyt c from its acid molten globule state to neutral pH state under high protein and ion concentrations. The amount of oligomeric cyt c obtained depended on the nature of the anion (chaotropic or kosmotropic) in the solution: ClO4(-) (oligomers, 11% ± 2% (heme unit)), SCN(-) (10% ± 2%), I(-) (6% ± 2%), NO3(-) (3% ± 1%), Br(-) (2% ± 1%), Cl(-) (2% ± 1%), and SO4(2-) (3% ± 1%) for refolding of 2 mM cyt c (anion concentration 125 mM). Dimeric cyt c obtained by refolding from the molten globule state exhibited a domain-swapped structure, in which the C-terminal α-helices were exchanged between protomers. According to small-angle X-ray scattering measurements, approximately 25% of the cyt c molecules were dimerized in the molten globule state containing 125 mM ClO4(-). These results indicate that a certain amount of molten globule state oligomers of cyt c convert to domain-swapped oligomers during refolding and that the intermolecular interactions necessary for domain swapping are present in the molten globule state.
PubMed: 24981551
DOI: 10.1021/bi500497s
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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